title: Crystallization and preliminary structural characterization of the two actin isoforms of the malaria parasite.
abstract: Malaria is a devastating disease caused by apicomplexan parasites of the genus Plasmodium that use a divergent actin-powered molecular motor for motility and invasion. Plasmodium actin differs from canonical actins in sequence, structure and function. Here, the purification, crystallization and secondary-structure analysis of the two Plasmodium actin isoforms are presented. The recombinant parasite actins were folded and could be purified to homogeneity. Plasmodium actins I and II were crystallized in complex with the gelsolin G1 domain; the crystals diffracted to resolutions of 1.19 and 2.2 Å and belonged to space groups P2₁2₁2₁ and P2₁, respectively, each with one complex in the asymmetric unit.
authors.affiliation: Department of Biochemistry, University of Oulu, PO Box 3000, 90014 Oulu, Finland.
authors.forename: Saligram Prabhakar
authors.initials: SP
authors.lastname: Bhargav
authors.forename: Juha
authors.initials: J
authors.lastname: Vahokoski
authors.forename: Esa-Pekka
authors.initials: EP
authors.lastname: Kumpula
authors.forename: Inari
authors.initials: I
authors.lastname: Kursula
mesh_terms: D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008288:Malaria / Q000469:parasitology*; D051379:Mice; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000378:metabolism*; D020033:Protein Isoforms; D015800:Protozoan Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000096:biosynthesis
chemical_list: D000199:Actins; D020033:Protein Isoforms; D015800:Protozoan Proteins; D011994:Recombinant Proteins
keywords: Plasmodium; actin; circular-dichroism spectroscopy; malaria; protein–protein complex